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弥合肌质间隙:骨骼肌兴奋-收缩偶联的最新进展

Bridging the myoplasmic gap: recent developments in skeletal muscle excitation-contraction coupling.

作者信息

Bannister Roger A

机构信息

Department of Physiology and Biophysics, School of Medicine, University of Colorado at Denver and Health Sciences Center, RC-1, North Tower, P18-7130, Mail Stop F8307, 12800 E. 19th St, Aurora, CO 80045, USA.

出版信息

J Muscle Res Cell Motil. 2007;28(4-5):275-83. doi: 10.1007/s10974-007-9118-5. Epub 2007 Sep 26.

DOI:10.1007/s10974-007-9118-5
PMID:17899404
Abstract

Conformational coupling between the L-type voltage-gated Ca(2+) channel (or 1,4-dihydropyridine receptor; DHPR) and the ryanodine-sensitive Ca(2+) release channel of the sarcoplasmic reticulum (RyR1) is the mechanistic basis for excitation-contraction (EC) coupling in skeletal muscle. In this article, recent findings regarding the roles of the individual cytoplasmic domains (the amino- and carboxyl-termini, cytoplasmic loops I-II, II-III, and III-IV) of the DHPR alpha(1S) subunit in bi-directional communication with RyR1 will be discussed.

摘要

L型电压门控钙通道(或1,4-二氢吡啶受体;DHPR)与肌浆网的兰尼碱敏感钙释放通道(RyR1)之间的构象偶联是骨骼肌兴奋-收缩(EC)偶联的机制基础。在本文中,将讨论关于DHPR α(1S)亚基的各个胞质结构域(氨基和羧基末端、胞质环I-II、II-III和III-IV)在与RyR1双向通讯中作用的最新发现。

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Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy.Stac3 是兴奋-收缩偶联机制的一个组成部分,在美洲原住民肌病中发生突变。
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